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| | <StructureSection load='6tqd' size='340' side='right'caption='[[6tqd]], [[Resolution|resolution]] 1.48Å' scene=''> | | <StructureSection load='6tqd' size='340' side='right'caption='[[6tqd]], [[Resolution|resolution]] 1.48Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[6tqd]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/Eco27 Eco27]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6TQD OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6TQD FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6tqd]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_O127:H6_str._E2348/69 Escherichia coli O127:H6 str. E2348/69]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6TQD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6TQD FirstGlance]. <br> |
| | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BR:BROMIDE+ION'>BR</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=PG4:TETRAETHYLENE+GLYCOL'>PG4</scene></td></tr> | | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BR:BROMIDE+ION'>BR</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=PG4:TETRAETHYLENE+GLYCOL'>PG4</scene></td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[6tpl|6tpl]]</div></td></tr>
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=6tqd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6tqd OCA], [https://pdbe.org/6tqd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6tqd RCSB], [https://www.ebi.ac.uk/pdbsum/6tqd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6tqd ProSAT]</span></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">eae, eaeA, E2348C_3939 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=574521 ECO27])</td></tr>
| + | |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=6tqd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6tqd OCA], [http://pdbe.org/6tqd PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6tqd RCSB], [http://www.ebi.ac.uk/pdbsum/6tqd PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6tqd ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/EAE_ECO27 EAE_ECO27]] Necessary for the production of attaching and effacing lesions on tissue culture cells. Believed to mediate adherence. | + | [https://www.uniprot.org/uniprot/EAE_ECO27 EAE_ECO27] Necessary for the production of attaching and effacing lesions on tissue culture cells. Believed to mediate adherence. |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Eco27]] | + | [[Category: Escherichia coli O127:H6 str. E2348/69]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Leo, J C]] | + | [[Category: Leo JC]] |
| - | [[Category: Morth, J P]] | + | [[Category: Morth JP]] |
| - | [[Category: Weikum, J]] | + | [[Category: Weikum J]] |
| - | [[Category: Adhesion]]
| + | |
| - | [[Category: Bacterial ig domain]]
| + | |
| - | [[Category: Big domain]]
| + | |
| - | [[Category: Cell adhesion]]
| + | |
| - | [[Category: Intimin]]
| + | |
| - | [[Category: Passenger domain]]
| + | |
| Structural highlights
Function
EAE_ECO27 Necessary for the production of attaching and effacing lesions on tissue culture cells. Believed to mediate adherence.
Publication Abstract from PubMed
Enterohemorrhagic and enteropathogenic Escherichia coli are among the most important food-borne pathogens, posing a global health threat. The virulence factor intimin is essential for the attachment of pathogenic E. coli to the intestinal host cell. Intimin consists of four extracellular bacterial immunoglobulin-like (Big) domains, D00-D2, extending into the fifth lectin subdomain (D3) that binds to the Tir-receptor on the host cell. Here, we present the crystal structures of the elusive D00-D0 domains at 1.5 A and D0-D1 at 1.8 A resolution, which confirms that the passenger of intimin has five distinct domains. We describe that D00-D0 exhibits a higher degree of rigidity and D00 likely functions as a juncture domain at the outer membrane-extracellular medium interface. We conclude that D00 is a unique Big domain with a specific topology likely found in a broad range of other inverse autotransporters. The accumulated data allows us to model the complete passenger of intimin and propose functionality to the Big domains, D00-D0-D1, extending directly from the membrane.
The extracellular juncture domains in the intimin passenger adopt a constitutively extended conformation inducing restraints to its sphere of action.,Weikum J, Kulakova A, Tesei G, Yoshimoto S, Jaegerum LV, Schutz M, Hori K, Skepo M, Harris P, Leo JC, Morth JP Sci Rep. 2020 Dec 4;10(1):21249. doi: 10.1038/s41598-020-77706-7. PMID:33277518[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Weikum J, Kulakova A, Tesei G, Yoshimoto S, Jaegerum LV, Schutz M, Hori K, Skepo M, Harris P, Leo JC, Morth JP. The extracellular juncture domains in the intimin passenger adopt a constitutively extended conformation inducing restraints to its sphere of action. Sci Rep. 2020 Dec 4;10(1):21249. doi: 10.1038/s41598-020-77706-7. PMID:33277518 doi:http://dx.doi.org/10.1038/s41598-020-77706-7
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